Engineered xyloglucan specificity in a carbohydrate-binding module.

Lavinia Cicortas Gunnarsson; Qi Zhou; Cedric Montanier; Eva Nordberg Karlsson; Harry Brumer; Mats Ohlin

doi:10.1093/glycob/cwl038

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Engineered xyloglucan specificity in a carbohydrate-binding module.

Lavinia Cicortas Gunnarsson·Qi Zhou·Cedric Montanier·Eva Nordberg Karlsson·Harry Brumer·Mats Ohlin

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Abstract

The field of plant cell wall biology is constantly growing and consequently so is the need for more sensitive and specific probes for individual wall components. Xyloglucan is a key polysaccharide widely distributed in the plant kingdom in both structural and storage tissues that exist in both fucosylated and non-fucosylated variants. Presently, the only xyloglucan marker available is the monoclonal antibody CCRC-M1 that is specific to terminal alpha-1,2-linked fucosyl residues on xyloglucan oligo- and polysaccharides. As a viable alternative to searches for natural binding proteins or creation of new monoclonal antibodies, an approach to select xyloglucan-specific binding proteins from a combinatorial library of the carbohydrate-binding module, CBM4-2, from xylanase Xyn10A of Rhodothermus marinus is described. Using phage display technology in combination with a chemoenzymatic method to anchor xyloglucan to solid supports, the selection of xyloglucan-binding modules with no detectable residual wild-type xylan and beta-glucan-binding ability was achieved.

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Amino Acid Sequence Biotin Endo-1,4-beta Xylanases Fucose Glucans Molecular Sequence Data Peptide Library Protein Binding Protein Engineering Rhodothermus Sequence Analysis, Protein Substrate Specificity Xylans Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

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Lavinia Cicortas Gunnarsson, Qi Zhou, Cedric Montanier, Eva Nordberg Karlsson, Harry Brumer, Mats Ohlin. 2006-08-10. Engineered xyloglucan specificity in a carbohydrate-binding module.. https://doi.org/10.1093/glycob%2Fcwl038

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